ID   H2A2C_MOUSE             Reviewed;         129 AA.
AC   Q64523; Q8CGP3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Histone H2A type 2-C;
DE   AltName: Full=H2A-clustered histone 20 {ECO:0000312|MGI:MGI:2448316};
DE   AltName: Full=H2a-613B;
GN   Name=H2ac20 {ECO:0000312|MGI:MGI:2448316};
GN   Synonyms=Hist2h2ab, Hist2h2ac {ECO:0000312|MGI:MGI:2448316};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=8858345; DOI=10.1101/gr.6.8.702;
RA   Wang Z.-F., Tisovec R., Debry R.W., Frey M.R., Matera A.G., Marzluff W.F.;
RT   "Characterization of the 55-kb mouse histone gene cluster on chromosome
RT   3.";
RL   Genome Res. 6:702-714(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12408966; DOI=10.1016/s0888-7543(02)96850-3;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
RN   [3]
RP   UBIQUITINATION AT LYS-120.
RX   PubMed=15525528; DOI=10.1016/j.devcel.2004.10.005;
RA   de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R.,
RA   Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N.;
RT   "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to
RT   heritable gene silencing and X inactivation.";
RL   Dev. Cell 7:663-676(2004).
RN   [4]
RP   UBIQUITINATION AT LYS-120.
RX   PubMed=15509584; DOI=10.1074/jbc.c400493200;
RA   Fang J., Chen T., Chadwick B., Li E., Zhang Y.;
RT   "Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes
RT   and is involved in initiation of X inactivation.";
RL   J. Biol. Chem. 279:52812-52815(2004).
RN   [5]
RP   METHYLATION AT ARG-4.
RX   PubMed=16699504; DOI=10.1038/ncb1413;
RA   Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,
RA   Kouzarides T., Surani M.A.;
RT   "Blimp1 associates with Prmt5 and directs histone arginine methylation in
RT   mouse germ cells.";
RL   Nat. Cell Biol. 8:623-630(2006).
RN   [6]
RP   CROTONYLATION AT LYS-37 AND LYS-119.
RX   PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA   Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA   Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J.,
RA   Ye Y., Khochbin S., Ren B., Zhao Y.;
RT   "Identification of 67 histone marks and histone lysine crotonylation as a
RT   new type of histone modification.";
RL   Cell 146:1016-1028(2011).
RN   [7]
RP   HYDROXYBUTYRYLATION AT LYS-6; LYS-10; LYS-37; LYS-75; LYS-76; LYS-96 AND
RP   LYS-119.
RX   PubMed=24681537; DOI=10.1038/nchembio.1497;
RA   Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A.,
RA   Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA   Khochbin S., Zhao Y.;
RT   "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT   mark.";
RL   Nat. Chem. Biol. 10:365-370(2014).
RN   [8]
RP   METHYLATION AT GLN-105.
RX   PubMed=24352239; DOI=10.1038/nature12819;
RA   Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J.,
RA   Nielsen M.L., Kouzarides T.;
RT   "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated
RT   modification.";
RL   Nature 505:564-568(2014).
RN   [9]
RP   HYDROXYBUTYRYLATION AT LYS-6; LYS-37; LYS-120 AND LYS-125.
RX   PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA   Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA   Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA   Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA   White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT   "Metabolic regulation of gene expression by histone lysine beta-
RT   hydroxybutyrylation.";
RL   Mol. Cell 62:194-206(2016).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone code, and nucleosome remodeling.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC       each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC       two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC       DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- PTM: Deiminated on Arg-4 in granulocytes upon calcium entry.
CC       {ECO:0000250|UniProtKB:P0C0S8}.
CC   -!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and
CC       RNF2/RING2 complex gives a specific tag for epigenetic transcriptional
CC       repression and participates in X chromosome inactivation of female
CC       mammals. It is involved in the initiation of both imprinted and random
CC       X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome
CC       chromatin. Ubiquitination of H2A functions downstream of methylation of
CC       'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be
CC       induced by ultraviolet and may be involved in DNA repair. Following DNA
CC       double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63'
CC       linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases
CC       RNF8 and RNF168, leading to the recruitment of repair proteins to sites
CC       of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and
CC       H2AK15Ub, respectively) in response to DNA damage is initiated by
CC       RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-
CC       linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to
CC       extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by
CC       USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after
CC       damaged DNA is repaired (By similarity). H2AK119Ub and ionizing
CC       radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and
CC       H2AK15Ub) are distinct events. {ECO:0000250|UniProtKB:P0C0S8,
CC       ECO:0000269|PubMed:15509584, ECO:0000269|PubMed:15525528,
CC       ECO:0000269|PubMed:24352239}.
CC   -!- PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis.
CC       Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses
CC       transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by
CC       RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is
CC       present in the regulatory region of many tumor suppresor genes and
CC       down-regulates their transcription. {ECO:0000250|UniProtKB:P0C0S8}.
CC   -!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may
CC       play a crucial role in the germ-cell lineage.
CC       {ECO:0000269|PubMed:16699504}.
CC   -!- PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is
CC       specifically dedicated to polymerase I. It is present at 35S ribosomal
CC       DNA locus and impairs binding of the FACT complex.
CC       {ECO:0000269|PubMed:24352239}.
CC   -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC       marks testis-specific genes in post-meiotic cells, including X-linked
CC       genes that escape sex chromosome inactivation in haploid cells.
CC       Crotonylation marks active promoters and enhancers and confers
CC       resistance to transcriptional repressors. It is also associated with
CC       post-meiotically activated genes on autosomes.
CC       {ECO:0000269|PubMed:21925322}.
CC   -!- PTM: Hydroxybutyrylation of histones is induced by starvation.
CC       {ECO:0000269|PubMed:27105115}.
CC   -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC       directly derived from endogenous or exogenous lactate, leading to
CC       stimulates gene transcription. {ECO:0000250|UniProtKB:P0C0S5}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; U62673; AAB04768.1; -; Genomic_DNA.
DR   EMBL; AY158922; AAO06232.2; -; Genomic_DNA.
DR   EMBL; AY158923; AAO06233.1; -; Genomic_DNA.
DR   CCDS; CCDS17634.1; -.
DR   RefSeq; NP_783593.1; NM_175662.2.
DR   AlphaFoldDB; Q64523; -.
DR   SMR; Q64523; -.
DR   BioGRID; 235095; 11.
DR   IntAct; Q64523; 1.
DR   STRING; 10090.ENSMUSP00000088288; -.
DR   GlyGen; Q64523; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q64523; -.
DR   PhosphoSitePlus; Q64523; -.
DR   SwissPalm; Q64523; -.
DR   EPD; Q64523; -.
DR   jPOST; Q64523; -.
DR   MaxQB; Q64523; -.
DR   PaxDb; 10090-ENSMUSP00000088288; -.
DR   Pumba; Q64523; -.
DR   TopDownProteomics; Q64523; -.
DR   Antibodypedia; 34012; 189 antibodies from 20 providers.
DR   DNASU; 319176; -.
DR   Ensembl; ENSMUST00000090782.4; ENSMUSP00000088288.4; ENSMUSG00000068855.4.
DR   GeneID; 319176; -.
DR   KEGG; mmu:319176; -.
DR   UCSC; uc008qmi.2; mouse.
DR   AGR; MGI:2448316; -.
DR   CTD; 8338; -.
DR   MGI; MGI:2448316; H2ac20.
DR   VEuPathDB; HostDB:ENSMUSG00000068855; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   GeneTree; ENSGT00940000153118; -.
DR   HOGENOM; CLU_062828_3_1_1; -.
DR   InParanoid; Q64523; -.
DR   OMA; ATHSHEK; -.
DR   OrthoDB; 4830315at2759; -.
DR   PhylomeDB; Q64523; -.
DR   TreeFam; TF300137; -.
DR   Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR   Reactome; R-MMU-5689603; UCH proteinases.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR   Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   BioGRID-ORCS; 319176; 8 hits in 55 CRISPR screens.
DR   PRO; PR:Q64523; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q64523; Protein.
DR   Bgee; ENSMUSG00000068855; Expressed in uterus and 59 other cell types or tissues.
DR   ExpressionAtlas; Q64523; baseline and differential.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   PANTHER; PTHR23430; HISTONE H2A; 1.
DR   PANTHER; PTHR23430:SF42; HISTONE H2A TYPE 2-A; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Citrullination; DNA-binding; Hydroxylation;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   CHAIN           2..129
FT                   /note="Histone H2A type 2-C"
FT                   /id="PRO_0000227512"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   MOD_RES         2
FT                   /note="Phosphoserine; by RPS6KA5"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         4
FT                   /note="Citrulline; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         4
FT                   /note="Symmetric dimethylarginine; by PRMT5; alternate"
FT                   /evidence="ECO:0000305|PubMed:16699504"
FT   MOD_RES         6
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         6
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   MOD_RES         10
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         10
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         10
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   MOD_RES         37
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         37
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         37
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         75
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         76
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         96
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         96
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         96
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   MOD_RES         100
FT                   /note="N6-glutaryllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         105
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000269|PubMed:24352239"
FT   MOD_RES         119
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:24681537"
FT   MOD_RES         119
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:21925322"
FT   MOD_RES         119
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         120
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         120
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         120
FT                   /note="N6-glutaryllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   MOD_RES         121
FT                   /note="Phosphothreonine; by DCAF1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   MOD_RES         125
FT                   /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:27105115"
FT   MOD_RES         125
FT                   /note="N6-crotonyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S8"
FT   CROSSLNK        14
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   CROSSLNK        16
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q16777"
FT   CROSSLNK        120
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000269|PubMed:15509584,
FT                   ECO:0000269|PubMed:15525528"
SQ   SEQUENCE   129 AA;  13988 MW;  358AE20D1C531724 CRC64;
     MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YMAAVLEYLT
     AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK
     TESHKAKSK
//